Reference : Temperature-sensitive mutant in the vaccinia virus E6 protein produce virions that ar...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/10993/41445
Temperature-sensitive mutant in the vaccinia virus E6 protein produce virions that are transcriptionally inactive.
English
Boyd, Olga mailto [University of Luxembourg > Luxembourg Centre for Systems Biomedicine (LCSB) >]
Strahl, Audra L. [> >]
Rodeffer, Carson [> >]
Condit, Richard C. [> >]
Moussatche, Nissin [> >]
2010
Virology
399
2
221-30
Yes (verified by ORBilu)
International
0042-6822
1096-0341
United States
[en] Animals ; Cell Line ; Chlorocebus aethiops ; DNA, Viral/biosynthesis/genetics ; Hot Temperature ; Mutation ; Transcription, Genetic ; Vaccinia virus/genetics/metabolism/physiology ; Viral Core Proteins/genetics/metabolism ; Viral Plaque Assay ; Virion/genetics/metabolism/physiology ; Virus Attachment ; Virus Internalization ; Virus Replication
[en] The vaccinia virus E6R gene encodes a late protein that is packaged into virion cores. A temperature-sensitive mutant was used to study the role of this protein in viral replicative cycle. Cts52 has a P226L missense mutation in the E6R gene, shows a two-log reduction in plaque formation, but displays normal patterns of gene expression, late protein processing and DNA replication during infection. Mutant virions produced at 40 degrees C were similar in their morphology to wt virions grown at 40 degrees C. The particle to infectivity ratio was 50 times higher in purified Cts52 grown at 40 degrees C when compared to the mutant grown at permissive temperature. In vitro characterization of Cts-52 particles grown at 40 degrees C revealed no differences in protein composition or in DNA content and the mutant virions could bind and enter cells. However, core particles prepared from Cts52 grown at 40 degrees C failed to transcribe in vitro. Our results show that E6 in the virion has either a direct or an indirect role in viral transcription.
http://hdl.handle.net/10993/41445
Published by Elsevier Inc.

File(s) associated to this reference

Fulltext file(s):

FileCommentaryVersionSizeAccess
Open access
nihms-171035.pdfPublisher postprint1.7 MBView/Open

Bookmark and Share SFX Query

All documents in ORBilu are protected by a user license.